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Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany





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Abstract Activity-based protein profiling uses chemical probes that covalently attach to active enzyme targets. Probes with conventional tags have disadvantages, such as limited cell permeability or steric hindrance around the reactive group. A tandem labeling strategy with click chemistry is now widely used to study enzyme targets in situ and in vivo. Herein, the probes are reacted in live cells, whereas the ensuing detection by click chemistry takes place in cell lysates. We here make a comparison of the efficiency of the activity-based tandem labeling strategy by using CuI-catalyzed and strain-promoted click chemistry, different ligands and different lysis conditions. View Full-Text

Keywords: activity-based probes; cathepsins; click chemistry; proteases; protein modification activity-based probes; cathepsins; click chemistry; proteases; protein modification





Autor: Yinliang Yang, Xiaomeng Yang and Steven H. L. Verhelst *

Fuente: http://mdpi.com/



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